2024
COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites
Liao Y, Pang S, Li W, Shtengel G, Choi H, Schaefer K, Xu C, Lippincott-Schwartz J. COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites. Developmental Cell 2024, 59: 1410-1424.e4. PMID: 38593803, DOI: 10.1016/j.devcel.2024.03.027.Peer-Reviewed Original ResearchEndoplasmic reticulum exit sitesER exit sitesAmino acid starvationPurified recombinant componentsExit siteProtein sortingSecretory pathwayMammalian cellsNutrient stressCellular conditionsEndoplasmic reticulumGiant unilamellar vesiclesTubular outgrowthsESCRTMicroautophagyNutrient stressorsALG2COPIILysosomesPathwayMTOR inhibitionUnilamellar vesiclesRecombinant componentsFocused Ion Beam Scanning Electron MicroscopyIon beam scanning electron microscopy
2022
Quantification of Protein Exit at the Trans-Golgi Network
Tran M, Kim Y, von Blume J. Quantification of Protein Exit at the Trans-Golgi Network. Methods In Molecular Biology 2022, 2557: 583-594. PMID: 36512239, DOI: 10.1007/978-1-0716-2639-9_35.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkProtein exportSecretory pathwaySelective hooks (RUSH) systemCell biological approachesProtein of interestPulse-chase experimentsProtein exitProtein sortingExport kineticsCellular homeostasisProtein transportDifferent cargoesLive cellsBiological approachesRUSH systemProteinPathwayTraffickingHomeostasisExportCargoSortingCompartmentsCells
2021
The Spliced Leader RNA Silencing (SLS) Pathway in Trypanosoma brucei Is Induced by Perturbations of Endoplasmic Reticulum, Golgi Complex, or Mitochondrial Protein Factors: Functional Analysis of SLS-Inducing Kinase PK3
Okalang U, Bar-Ner B, Rajan K, Friedman N, Aryal S, Egarmina K, Hope R, Khazanov N, Senderowitz H, Alon A, Fass D, Michaeli S. The Spliced Leader RNA Silencing (SLS) Pathway in Trypanosoma brucei Is Induced by Perturbations of Endoplasmic Reticulum, Golgi Complex, or Mitochondrial Protein Factors: Functional Analysis of SLS-Inducing Kinase PK3. MBio 2021, 12: e02602-21. PMID: 34844425, PMCID: PMC8630539, DOI: 10.1128/mbio.02602-21.Peer-Reviewed Original ResearchConceptsSpliced leader RNA silencingER oxidoreductin 1Quiescin sulfhydryl oxidaseER-resident chaperone BiPMitochondrial protein importEndoplasmic reticulumProtein importChaperone BiPRNA silencingSpliced leader (SL) RNACausative agent of human African sleeping sicknessSulfhydryl oxidasePerturbation of endoplasmic reticulumSL RNA transcriptionInduction of programmed cell deathHuman African sleeping sicknessATP-binding domainPotential novel drug targetsParasite Trypanosoma bruceiSerine-threonine kinaseNovel drug targetsProtein sortingAfrican sleeping sicknessProtein translocationPhosphorylation eventsRetention Using Selective Hooks (RUSH) Cargo Sorting Assay for Protein Vesicle Tracking in HeLa Cells.
Pacheco-Fernandez N, Pakdel M, Von Blume J. Retention Using Selective Hooks (RUSH) Cargo Sorting Assay for Protein Vesicle Tracking in HeLa Cells. Bio-protocol 2021, 11: e3936. PMID: 33796610, PMCID: PMC8005885, DOI: 10.21769/bioprotoc.3936.Peer-Reviewed Original ResearchSecretory pathwaySelective hooks (RUSH) systemProtein sortingVesicle traffickingSpecific cargoCargo traffickingProtein cargoTrafficking dynamicsProtein dynamicsVesicle trackingBiotin additionHeLa cellsFluorescent vesiclesTraffickingSorting assaysPathwayCargoCellsProteinExcellent toolSuch studiesVesiclesBetter understandingRegulationSorting
2018
Activity of the SPCA1 Calcium Pump Couples Sphingomyelin Synthesis to Sorting of Secretory Proteins in the Trans-Golgi Network
Deng Y, Pakdel M, Blank B, Sundberg EL, Burd CG, von Blume J. Activity of the SPCA1 Calcium Pump Couples Sphingomyelin Synthesis to Sorting of Secretory Proteins in the Trans-Golgi Network. Developmental Cell 2018, 47: 464-478.e8. PMID: 30393074, PMCID: PMC6261503, DOI: 10.1016/j.devcel.2018.10.012.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkTGN membranesCell surface transportProtein sortingTrafficking pathwaysSecretion pathwaySecretory proteinsSphingomyelin synthesisSorting mechanismLipid synthesisProteinVesicular carriersCab45Sphingomyelin contentNew lipidSortingPrincipal functionMembranePathwayCore componentLipidsGolgiSurface transportExportActivity
2017
The where, what, and when of membrane protein degradation in neurons
Jin E, Kiral F, Hiesinger P. The where, what, and when of membrane protein degradation in neurons. Developmental Neurobiology 2017, 78: 283-297. PMID: 28884504, PMCID: PMC5816708, DOI: 10.1002/dneu.22534.Peer-Reviewed Original Research
2016
Newly synthesized and recycling pools of the apical protein gp135 do not occupy the same compartments
Stoops EH, Hull M, Caplan MJ. Newly synthesized and recycling pools of the apical protein gp135 do not occupy the same compartments. Traffic 2016, 17: 1272-1285. PMID: 27649479, PMCID: PMC5123909, DOI: 10.1111/tra.12449.Peer-Reviewed Original ResearchConceptsApical early endosomesPlasma membrane proteinsPolarized epithelial cellsApical recycling endosomesDistinct trafficking pathwaysSNAP-tag systemBasolateral membrane domainsProtein sortingApical proteinsRecycling endosomesTrafficking pathwaysGolgi networkProtein trafficMembrane domainsMembrane proteinsEarly endosomesPlasma membraneInitial traffickingEndosomesApical membraneProteinGp135Same compartmentEpithelial cellsTrafficking
2013
Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease.
Bertuccio CA, Caplan MJ. Polycystin-1C terminus cleavage and its relation with polycystin-2, two proteins involved in polycystic kidney disease. Medicina 2013, 73: 155-62. PMID: 23570767.Peer-Reviewed Original ResearchConceptsPolycystin-1Polycystin-2Autosomal dominant polycystic kidney diseaseTerminal cytoplasmic tailProtein sortingNormal tubulogenesisPolycystic kidney diseaseProtein functionCytoplasmic tailTerminal tailCommon genetic causeCystogenic processExtracellular matrixDifferentiation mechanismsCellular proliferationGenetic causeMultiple cleavagesDominant polycystic kidney diseasePathwayHigh proliferative rateCleavageProliferative rateSecretory characteristicsGenesTubulogenesis
2011
Lysosomal Trafficking, Antigen Presentation, and Microbial Killing Are Controlled by the Arf-like GTPase Arl8b
Garg S, Sharma M, Ung C, Tuli A, Barral D, Hava D, Veerapen N, Besra G, Hacohen N, Brenner M. Lysosomal Trafficking, Antigen Presentation, and Microbial Killing Are Controlled by the Arf-like GTPase Arl8b. Immunity 2011, 35: 182-193. PMID: 21802320, PMCID: PMC3584282, DOI: 10.1016/j.immuni.2011.06.009.Peer-Reviewed Original ResearchMeSH KeywordsADP-Ribosylation FactorsAntigen PresentationAntigensAntigens, CD1dCytokinesCytotoxicity, ImmunologicHeLa CellsHumansLymphocyte ActivationLysosomesNatural Killer T-CellsProtein BindingProtein TransportProteolipidsrab GTP-Binding Proteinsrab7 GTP-Binding ProteinsRNA, Small InterferingVesicular Transport ProteinsConceptsHomotypic fusion and vacuole protein sortingGTPase Arl8bMicrobial killingVacuole protein sortingPhagosome-lysosome fusionCargo traffickingProtein sortingArl8bShRNA librarySilenced cellsLysosomal traffickingPlasma membraneMolecular regulationImmunological screeningHost defenseLysosomesTraffickingAntigen presentationT cell activationCargo deliveryRegulationKillingCell activationImmunological functionsEffector
2007
Gaucher Disease: Forging a New Path to the Lysosome
Griffiths G. Gaucher Disease: Forging a New Path to the Lysosome. Cell 2007, 131: 647-649. PMID: 18022357, DOI: 10.1016/j.cell.2007.10.043.Peer-Reviewed Original Research
2001
High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †
Sankaran V, Klein D, Sachdeva M, Lemmon M. High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †. Biochemistry 2001, 40: 8581-8587. PMID: 11456498, DOI: 10.1021/bi010425d.Peer-Reviewed Original ResearchMeSH KeywordsBinding, CompetitiveBlood ProteinsCarrier ProteinsCation Transport ProteinsGlutathione TransferaseGuanine Nucleotide Exchange FactorsHeLa CellsHumansLiposomesMonosaccharide Transport ProteinsPhosphatidylinositol PhosphatesPhospholipidsPhosphoproteinsProtein BindingProtein Structure, TertiaryProteinsRecombinant Fusion ProteinsSymportersZinc FingersConceptsFYVE domainPH domainDomain oligomerizationSpecific PH domainsVacuolar protein sortingPleckstrin homology domainLipid headgroupsProtein sortingMembrane trafficHomology domainSpecific phosphoinositideLike domainEndosomal maturationHigh-affinity bindingPreferred lipidPhospholipase CPhosphoinositideIntact lipidsIntact phospholipidsOligomerizationDomainMembrane
2000
The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways
Amerik A, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways. Molecular Biology Of The Cell 2000, 11: 3365-3380. PMID: 11029042, PMCID: PMC14998, DOI: 10.1091/mbc.11.10.3365.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaAmino Acid SequenceBreast NeoplasmsCysteine EndopeptidasesEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportFemaleFungal ProteinsGenotypeHumansMolecular Sequence DataMultienzyme ComplexesMutagenesisProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificitySuppression, GeneticUbiquitin ThiolesteraseUbiquitinsVacuolesConceptsPrevacuolar compartmentDeubiquitinating enzymeVacuolar protein sorting (VPS) pathwayFluorescent proteinEndomembrane protein traffickingProtein sorting pathwaysUbiquitinated membrane proteinsVacuolar protein sortingClass E compartmentSpontaneous extragenic suppressorsGreen fluorescent proteinExtragenic suppressorsProtein sortingProtein traffickingProtein deubiquitinationUbiquitin recyclingPathway substrateE compartmentMembrane proteinsEndocytic pathwayUbiquitinated intermediatesDifferent genesMultivesicular bodiesNuclear distributionUnanticipated connectionsVisualizing protein dynamics in yeast with green fluorescent protein
Burd C. Visualizing protein dynamics in yeast with green fluorescent protein. Methods In Enzymology 2000, 327: 61-69. PMID: 11044974, DOI: 10.1016/s0076-6879(00)27267-4.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein dynamicsUse of GFPFluorescent proteinYeast cell biologyProtein sortingRNA localizationIndividual cellular componentsChromosomal dynamicsProtein localizationKinase signalingCell biologyMutant strainMolecular tagsCellular componentsYeastProteinNucleocytoplasmicBroad arrayLocalizationSignalingBiologySortingMajor impactTags
1997
A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast.
Burd C, Peterson M, Cowles C, Emr S. A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast. Molecular Biology Of The Cell 1997, 8: 1089-1104. PMID: 9201718, PMCID: PMC305716, DOI: 10.1091/mbc.8.6.1089.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesBiological TransportCell CompartmentationCytoskeletal ProteinsEndosomesFungal ProteinsGolgi ApparatusGTP-Binding ProteinsMacromolecular SubstancesMembrane FusionMembrane ProteinsProtein BindingQa-SNARE Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipVacuolesVesicular Transport ProteinsZincConceptsVacuolar protein sortingProtein sortingVPS pathwayEndosome transportSevere synthetic growth defectVacuolar protein sorting (VPS) genesVacuolar protein sorting (VPS) pathwaySynthetic growth defectsProtein sorting pathwaysZinc finger motifsRab family GTPaseCoiled-coil motifLocalization of proteinsSite-directed mutationsSDS-resistant complexesDominant negative mutationTsf phenotypeTsf mutationsFinger motifVesicle receptorsEndosome traffickingVacuole inheritanceVac1pVacuolar proteinTrans-GolgiMembrane polarity in epithelial cells: protein sorting and establishment of polarized domains
Caplan MJ. Membrane polarity in epithelial cells: protein sorting and establishment of polarized domains. American Journal Of Physiology 1997, 272: f425-f429. PMID: 9140041, DOI: 10.1152/ajprenal.1997.272.4.f425.Peer-Reviewed Original ResearchConceptsTransport proteinsEpithelial cellsDistinct surface domainsEpithelial cell typesProtein sortingBiological specializationCellular pathwaysPlasma membranePolarized epitheliumElegant networkMembrane polarityCell typesBasolateral surfaceDistinct populationsProteinBasolateral portionPhysiological propertiesSurface domainsCellsAbsolute prerequisiteDomainPlasmalemmaPathwaySortingMembraneProtein sorting and secretion during CTL killing
Griffiths G. Protein sorting and secretion during CTL killing. Seminars In Immunology 1997, 9: 109-115. PMID: 9194221, DOI: 10.1006/smim.1997.0059.Peer-Reviewed Original Research
1996
Secretory lysosomes — a special mechanism of regulated secretion in haemopoietic cells
Griffiths G. Secretory lysosomes — a special mechanism of regulated secretion in haemopoietic cells. Trends In Cell Biology 1996, 6: 329-332. PMID: 15157429, DOI: 10.1016/0962-8924(96)20031-5.Peer-Reviewed Original ResearchSecretory lysosomesRegulate protein sortingProtein sortingSecretory organellesSecretory proteinsHaemopoietic lineagesCytotoxic T lymphocytesSecretory granulesLysosomal hydrolasesLysosomesSecretory mechanismLineagesMutantsCellsOrganellesSortingSecretionHydrolaseHaemopoietic cellsProteinT lymphocytesMechanismA Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins
Burd C, Mustol P, Schu P, Emr S. A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins. Molecular And Cellular Biology 1996, 16: 2369-2377. PMID: 8628304, PMCID: PMC231225, DOI: 10.1128/mcb.16.5.2369.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsCarrier ProteinsCloning, MolecularFungal ProteinsGenes, FungalGenetic Complementation TestGuanine Nucleotide Exchange FactorsHumansMammalsMolecular Sequence DataMutagenesisPolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTemperatureVacuolesVesicular Transport ProteinsConceptsVacuolar protein sortingProtein sortingVacuolar proteinVPS pathwayVacuolar protein sorting (VPS) genesTemperature-sensitive growth defectTemperature-conditional alleleVacuolar protein precursorsFamily of proteinsSecretion of proteinsRab GTPaseRA-binding proteinsTransport vesiclesYeast proteinsHomology domainYeast SaccharomycesGrowth defectHuman proteinsVps9pDNA sequencesGene productsCytosolic proteinsNonpermissive temperatureCarboxypeptidase YIntracellular transportPolarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗)
Ahn J, Mundigl O, Muth T, Rudnick G, Caplan M. Polarized Expression of GABA Transporters in Madin-Darby Canine Kidney Cells and Cultured Hippocampal Neurons (∗). Journal Of Biological Chemistry 1996, 271: 6917-6924. PMID: 8636119, DOI: 10.1074/jbc.271.12.6917.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAxonsBase SequenceCarrier ProteinsCell LineDNA PrimersDNA, ComplementaryDogsGABA Plasma Membrane Transport Proteinsgamma-Aminobutyric AcidHippocampusKidneyMembrane ProteinsMembrane Transport ProteinsMicroinjectionsMolecular Sequence DataNeuronsOrganic Anion TransportersConceptsMadin-Darby canine kidney cellsCanine kidney cellsMDCK cellsBetaine transporterMembrane protein sortingAmino acid sequence identityApical membraneCell surface biotinylationGAT-2GABA transporterKidney cellsGamma-aminobutyric acid transporterEpithelial cellsProtein sortingGAT-1Polarized neuronsSurface biotinylationSequence identityAcid transportersCultured hippocampal neuronsHippocampal neuronsPolarized expressionCell typesTransporter GAT-1Basolateral surface
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